Unknown

Dataset Information

0

Structures of human primosome elongation complexes.


ABSTRACT: The synthesis of RNA-DNA primer by primosome requires coordination between primase and DNA polymerase α subunits, which is accompanied by unknown architectural rearrangements of multiple domains. Using cryogenic electron microscopy, we solved a 3.6 Å human primosome structure caught at an early stage of RNA primer elongation with deoxynucleotides. The structure confirms a long-standing role of primase large subunit and reveals new insights into how primosome is limited to synthesizing short RNA-DNA primers.

SUBMITTER: He Q 

PROVIDER: S-EPMC10268227 | biostudies-literature | 2023 May

REPOSITORIES: biostudies-literature

altmetric image

Publications

Structures of human primosome elongation complexes.

He Qixiang Q   Baranovskiy Andrey G AG   Morstadt Lucia M LM   Lisova Alisa E AE   Babayeva Nigar D ND   Lusk Benjamin L BL   Lim Ci Ji CJ   Tahirov Tahir H TH  

Nature structural & molecular biology 20230417 5


The synthesis of RNA-DNA primer by primosome requires coordination between primase and DNA polymerase α subunits, which is accompanied by unknown architectural rearrangements of multiple domains. Using cryogenic electron microscopy, we solved a 3.6 Å human primosome structure caught at an early stage of RNA primer elongation with deoxynucleotides. The structure confirms a long-standing role of primase large subunit and reveals new insights into how primosome is limited to synthesizing short RNA-  ...[more]

Similar Datasets

| S-EPMC5333051 | biostudies-literature
| S-EPMC9800341 | biostudies-literature
| S-EPMC3648537 | biostudies-literature
| S-EPMC9226528 | biostudies-literature
2022-12-16 | GSE173374 | GEO
| S-EPMC4858955 | biostudies-literature
| S-EPMC3172387 | biostudies-literature
| S-EPMC2443823 | biostudies-literature
| S-EPMC3938583 | biostudies-literature
| S-EPMC1945215 | biostudies-literature